ISOLATION AND PARTIALLY PURIFICATION OF PROTEIN DISULFIDA ISOMERASE FROM Saccharomyces cerevisiae [pUKC470]

Wahjudi, Mariana and Sindumarta, Muliawati and Natalia, Dessy (2004) ISOLATION AND PARTIALLY PURIFICATION OF PROTEIN DISULFIDA ISOMERASE FROM Saccharomyces cerevisiae [pUKC470]. In: THE 3rd INDONESIAN BIOTECHNOLOGY CONFERENCE 2004 : AN INTERNATIONAL CONFERENCE AND EXHIBITION, 1-3 desember 2004, Bali.

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Abstract

Protein disulphide isomerase (PDI) is a multi-enzyme involved in catalyzing redox and isomerization reactions of clisulphide bonds in secretory proteins. This investigation is focused on the isolation and partially purification of PDI from Saccharomyces cerevisiae [p UKC4 70] in order to elucidate mechanism of action of PDI by characterizing kinetics of the enzyme. The specific activity of PDI isolated from transformant increased by 17 fold compared to the wild type Saccharomyces cerevisiae W303. The purification of PDI from transformant using ammonium sulphate fractionation followed by ion exchange chromatography on DEAE-Sephacel revealed that the specific activity of PDI increased to 255.28 unit per mg, a degree of purity 137 fold compared to the cells free extract, and yield of 41 %.

Item Type: Conference or Workshop Item (Paper)
Uncontrolled Keywords: DEAE-. dietilaminoetil-; PDf" Protein disulphide isomerase; Saccharomyces cerevisiae (pUKC470}
Subjects: R Medicine > R Medicine (General)
Divisions: Faculty of Pharmacy > Department of Pharmacy
Depositing User: Eko Setiawan 194014
Date Deposited: 10 Jun 2015 02:22
Last Modified: 25 Apr 2016 07:57
URI: http://repository.ubaya.ac.id/id/eprint/24577

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